Search results for " Non-Histone"

showing 7 items of 27 documents

Conserved chromosomal clustering of genes governed by chromatin regulators in Drosophila

2008

Transcriptional analysis of chromatin regulator mutants in Drosophila melanogaster identified clusters of functionally related genes conserved in other insect species.

Model organismsanimal structuresTranscription GeneticEvolutionChromosomal Proteins Non-HistoneDrosòfila melanogasterGenome studiesDevelopmentBiologyNon-histone proteinAnimalsDrosophila ProteinsDrosòfila -- GenèticaTranscription factorGeneGeneticsMicroarray analysis techniquesResearchGene Expression ProfilingMutació (Biologia)fungiNuclear Proteinsbiology.organism_classificationChromatin Assembly and DisassemblyChromatinHistoneDrosophila melanogasterDrosofila melanogasterGene Expression RegulationMultigene Familybiology.proteinDrosophila melanogasterDrosophila ProteinGenètica del desenvolupamentTranscription FactorsGenome Biology
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A multifunctional bicupin serves as precursor for a chromosomal protein of Pisum sativum seeds.

2005

The fact that the psp54 gene codes for p16, a seed chromatin protein of Pisum sativum, has been described previously. In the present paper it is shown that p54, the p16 precursor, also exists as a free polypeptide in pea and that it also yields p38, a second polypeptide from the N-terminal region of p54, which is co-localized at a subcellular level with p16. By using antibodies against pea p16 and p38, it was found that these proteins are present in the members of the tribe Viciae examined. Sequence analysis and 3D modelling indicates that p54 proteins belong to the cupin superfamily, and that they are related to sucrose binding proteins and, to a lesser extent, to vicilin-type seed storage…

Models MolecularPhysiologySequence analysisChromosomal Proteins Non-HistoneMolecular Sequence DataPlant ScienceResponse ElementsDNA-binding proteinPisumSativumGene Expression Regulation PlantSequence Analysis ProteinGene expressionStorage proteinAmino Acid SequenceRNA MessengerProtein PrecursorsPromoter Regions GeneticGenePlant Proteinschemistry.chemical_classificationMessenger RNAbiologyPeasfood and beveragesbiology.organism_classificationBiochemistrychemistryMultigene FamilyProtein BiosynthesisSeedsProtein Processing Post-TranslationalSequence AlignmentAbscisic AcidJournal of experimental botany
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The telomeric Cdc13-Stn1-Ten1 complex regulates RNA polymerase II transcription

2019

Advance article.

S phase transcribed genesTranscription GeneticChromosomal Proteins Non-HistoneCell Cycle ProteinsRNA polymerase IIBur1[SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]Genome Integrity Repair and ReplicationS Phase0302 clinical medicineTranscription (biology)Gene Expression Regulation FungalTranscriptional regulation0303 health sciencesCdc13-Stn1-Ten1biology030302 biochemistry & molecular biologyTranscription regulationRNA pol IIChromatinCyclin-Dependent KinasesCell biologyTelomeres030220 oncology & carcinogenesisRNA Polymerase IITranscriptional Elongation FactorsSaccharomyces cerevisiae ProteinsDNA polymerase IITelomere-Binding ProteinsSaccharomyces cerevisiae[SDV.CAN]Life Sciences [q-bio]/CancerSaccharomyces cerevisiaeCST complex03 medical and health sciencesGeneticsBudding yeastGenomesGene030304 developmental biologyHmo1RNA[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologyPromoterbiology.organism_classificationCromosomesTelomerebiology.proteinSpt5Cyclin-Dependent Kinase-Activating Kinase
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Crystallization and preliminary X-ray studies of mouse centrin1.

2005

The expression, purification, crystallization and preliminary X-ray diffraction studies of mouse centrin1 are reported. Centrins belong to a family of Ca{sup 2+}-binding EF-hand proteins that play a fundamental role in centrosome duplication and the function of cilia. To shed light on the structure–function relationship of these proteins, mouse centrin1 has been crystallized. The mouse centrin1 has been expressed in Escherichia coli as a GST-centrin fusion protein containing a thrombin protease cleavage site between the fusion partners. Two constructs with different linking-sequence lengths were expressed and purified. Thrombin cleavage yielded functional centrin1 and N-terminally extended …

StereochemistryChromosomal Proteins Non-HistoneMolecular Sequence DataBiophysicsmacromolecular substancesCleavage (embryo)Crystallography X-RayBiochemistrylaw.inventionchemistry.chemical_compoundMiceStructure-Activity RelationshipThrombinStructural BiologylawGeneticsmedicineEscherichia coliAnimalsCentrosome duplicationAmino Acid SequenceCrystallizationDose-Response Relationship DrugCalcium-Binding ProteinsSpace groupCondensed Matter PhysicsFusion proteinRecombinant ProteinsCrystallographyenzymes and coenzymes (carbohydrates)KineticschemistryCrystallization CommunicationsX-ray crystallographybiological scienceshealth occupationsbacteriaCrystallizationEthylene glycolmedicine.drugActa crystallographica. Section F, Structural biology and crystallization communications
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Nuclear aggregation of olfactory receptor genes governs their monogenic expression.

2012

SummaryGene positioning and regulation of nuclear architecture are thought to influence gene expression. Here, we show that, in mouse olfactory neurons, silent olfactory receptor (OR) genes from different chromosomes converge in a small number of heterochromatic foci. These foci are OR exclusive and form in a cell-type-specific and differentiation-dependent manner. The aggregation of OR genes is developmentally synchronous with the downregulation of lamin b receptor (LBR) and can be reversed by ectopic expression of LBR in mature olfactory neurons. LBR-induced reorganization of nuclear architecture and disruption of OR aggregates perturbs the singularity of OR transcription and disrupts the…

Transcription GeneticCytoplasmic and NuclearChromosomal Proteins Non-HistoneDown-RegulationReceptors Cytoplasmic and NuclearLamin B receptorBiologyReceptors OdorantMedical and Health SciencesGeneral Biochemistry Genetics and Molecular BiologyFluorescenceOlfactory Receptor NeuronsArticle03 medical and health sciencesMice0302 clinical medicineDownregulation and upregulationGeneticTranscription (biology)HeterochromatinGene expressionReceptorsmedicineGeneticsAnimalsGeneIn Situ HybridizationIn Situ Hybridization Fluorescence030304 developmental biologyRegulation of gene expressionCell Nucleus0303 health sciencesOlfactory receptorBiochemistry Genetics and Molecular Biology(all)Neurosciencesta1182Non-HistoneBiological SciencesCell biologyChromosomal Proteinsmedicine.anatomical_structureOdorantGene Expression RegulationEctopic expressionTranscription030217 neurology & neurosurgeryDevelopmental BiologyCell
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Tracing the origin of the compensasome: evolutionary history of DEAH helicase and MYST acetyltransferase gene families.

2001

Dosage compensation in Drosophila is mediated by a complex of proteins and RNAs called the "compensasome." Two of the genes that encode proteins of the complex, maleless (mle) and males-absent-on-the-first (mof), respectively, belong to the DEAH helicase and MYST acetyltransferase gene families. We performed comprehensive phylogenetic and structural analyses to determine the evolutionary histories of these two gene families and thus to better understand the origin of the compensasome. All of the members of the DEAH and MYST families of the completely sequenced Saccharomyces cerevisiae and Caenorhabditis elegans genomes, as well as those so far (June 2000) found in Drosophila melanogaster (f…

animal structuresChromosomal Proteins Non-HistoneMolecular Sequence DataBiologyEvolution MolecularAcetyltransferasesGeneticsGene familyAnimalsDrosophila ProteinsAmino Acid SequenceMolecular BiologyGeneEcology Evolution Behavior and SystematicsCaenorhabditis elegansPhylogenyHistone AcetyltransferasesGeneticsDosage compensationSequence Homology Amino AcidfungiDNA HelicasesHelicaseNuclear Proteinsbiology.organism_classificationRNA Helicase ACaenorhabditisDNA-Binding ProteinsMultigene Familybiology.proteinDrosophila melanogasterRNA HelicasesTranscription FactorsMolecular biology and evolution
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Light-dependent CK2-mediated phosphorylation of centrins regulates complex formation with visual G-protein.

2008

AbstractCentrins are Ca2+-binding EF-hand proteins. All four known centrin isoforms are expressed in the ciliary apparatus of photoreceptor cells. Cen1p and Cen2p bind to the visual G-protein transducin in a strictly Ca2+-dependent way, which is thought to regulate light driven movements of transducin between photoreceptor cell compartments. These relatively slow motile processes represent a novel paradigm in light adaptation of photoreceptor cells.Here we validated specific phosphorylation as a novel regulator of centrins in photoreceptors. Centrins were differentially phosphorylated during photoreceptor dark adaptation. Inhibitor treatments revealed protein kinase CK2 as the major protein…

genetic structuresLightG proteinVisionChromosomal Proteins Non-HistoneBlotting WesternDark AdaptationBiologySignal transductionMicrotubulesPhotoreceptor cellMass SpectrometryCa2+-binding proteinsSubstrate SpecificityRats Sprague-DawleyMiceHeterotrimeric G proteinmedicineAnimalsCiliaTransducinPhosphorylationProtein kinase ACasein Kinase IIFluorescent Antibody Technique IndirectMicroscopy ImmunoelectronMolecular BiologyCytoskeletonCiliumCalcium-Binding ProteinsCell BiologyCell biologyRatsMice Inbred C57BLmedicine.anatomical_structureCentrinPhosphorylationHeterotrimeric G-proteinCalciumCattleTransducinsense organsMolecular translocationPhotoreceptor Cells VertebrateProtein BindingBiochimica et biophysica acta
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